Components and Architecture of the Rhabdovirus Ribonucleoprotein Complex

Riedel, Christiane; Hennrich, Alexandru A; Conzelmann, Karl‐Klaus

doi:10.3390/v12090959

Cited by 21 publications

(16 citation statements)

References 92 publications

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“…The entry of lyssaviruses into host cells is mediated by their single type I transmembrane glycoprotein G. An N-terminal signal peptide directs synthesis of the protein into the ER, and after cleavage of the signal peptide, the nascent protein is anchored in the membrane by a single-pass alpha-helical transmembrane domain. A short cytoplasmic tail (CT) is involved in association with matrix protein (M)-coated viral ribonucleoproteins [ 17 ] at the site of virus envelope assembly and budding [ 18 , 19 ]. G trimers on the virion surface [ 20 , 21 ] can bind cellular receptors, which trigger virion endocytosis and pH-dependent membrane fusion [ 22 , 23 , 24 ].…”

Section: Resultsmentioning

confidence: 99%

Glycoproteins of Predicted Amphibian and Reptile Lyssaviruses Can Mediate Infection of Mammalian and Reptile Cells

Oberhuber

Schopf

Hennrich

et al. 2021

Viruses

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Lyssaviruses are neurotropic rhabdoviruses thought to be restricted to mammalian hosts, and to originate from bats. The identification of lyssavirus sequences from amphibians and reptiles by metatranscriptomics thus comes as a surprise and challenges the mammalian origin of lyssaviruses. The novel sequences of the proposed American tree frog lyssavirus (ATFLV) and anole lizard lyssavirus (ALLV) reveal substantial phylogenetic distances from each other and from bat lyssaviruses, with ATFLV being the most distant. As virus isolation has not been successful yet, we have here studied the functionality of the authentic ATFLV- and ALLV-encoded glycoproteins in the context of rabies virus pseudotype particles. Cryogenic electron microscopy uncovered the incorporation of the plasmid-encoded G proteins in viral envelopes. Infection experiments revealed the infectivity of ATFLV and ALLV G-coated RABV pp for a broad spectrum of cell lines from humans, bats, and reptiles, demonstrating membrane fusion activities. As presumed, ATFLV and ALLV G RABV pp escaped neutralization by human rabies immune sera. The present findings support the existence of contagious lyssaviruses in poikilothermic animals, and reveal a broad cell tropism in vitro, similar to that of the rabies virus.

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Section: Resultsmentioning

confidence: 99%

Glycoproteins of Predicted Amphibian and Reptile Lyssaviruses Can Mediate Infection of Mammalian and Reptile Cells

Oberhuber

Schopf

Hennrich

et al. 2021

Viruses

Self Cite

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“…In addition to a size-limiting mechanism, the number of VFs is also limited to a few per cell [ 78 ]. At this point, capsid/genome packages of the approximate size of the virion are ejected from the factories and transported via cytoskeleton to the membrane, with the participation of the matrix (M) protein [ 131 , 132 ], to bridge and interact with the intracellular domains of the viral membrane glycoproteins, which were synthesized in the ER, before exiting the cell [ 133 , 132 ]. In the case of nsNSVs, packages ejected from the VFs include the N-encapsidated genome and the structural proteins that will be part of the virion (L, polymerase cofactor/s and M protein) (referred to as “proto-nucleocapsids” in Fig 2B ).…”

Section: Biochemical Advantages Of Llps For Viral Factory Formation Function and Fatementioning

confidence: 99%

Deconstructing virus condensation

et al. 2021

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Viruses have evolved precise mechanisms for using the cellular physiological pathways for their perpetuation. These virus-driven biochemical events must be separated in space and time from those of the host cell. In recent years, granular structures, known for over a century for rabies virus, were shown to host viral gene function and were named using terms such as viroplasms, replication sites, inclusion bodies, or viral factories (VFs). More recently, these VFs were shown to be liquid-like, sharing properties with membrane-less organelles driven by liquid–liquid phase separation (LLPS) in a process widely referred to as biomolecular condensation. Some of the best described examples of these structures come from negative stranded RNA viruses, where micrometer size VFs are formed toward the end of the infectious cycle. We here discuss some basic principles of LLPS in connection with several examples of VFs and propose a view, which integrates viral replication mechanisms with the biochemistry underlying liquid-like organelles. In this view, viral protein and RNA components gradually accumulate up to a critical point during infection where phase separation is triggered. This yields an increase in transcription that leads in turn to increased translation and a consequent growth of initially formed condensates. According to chemical principles behind phase separation, an increase in the concentration of components increases the size of the condensate. A positive feedback cycle would thus generate in which crucial components, in particular nucleoproteins and viral polymerases, reach their highest levels required for genome replication. Progress in understanding viral biomolecular condensation leads to exploration of novel therapeutics. Furthermore, it provides insights into the fundamentals of phase separation in the regulation of cellular gene function given that virus replication and transcription, in particular those requiring host polymerases, are governed by the same biochemical principles.

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“…The genome itself is flanked by a 3′ leader and 5′ trailer region, which contain transcription and replication promoters in addition to N protein encapsidation signals [ 3 ]. Together, the five structural proteins produce the bullet-shaped virion characteristic of rhabdoviruses [ 6 ], and the structures of each protein have been solved [ 7 ]. The viral genome is coated and protected by the N protein [ 8 , 9 ].…”

Section: Vesicular Stomatitis Virusmentioning

confidence: 99%

Vesicular Stomatitis Virus: From Agricultural Pathogen to Vaccine Vector

et al. 2021

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Vesicular stomatitis virus (VSV), which belongs to the Vesiculovirus genus of the family Rhabdoviridae, is a well studied livestock pathogen and prototypic non-segmented, negative-sense RNA virus. Although VSV is responsible for causing economically significant outbreaks of vesicular stomatitis in cattle, horses, and swine, the virus also represents a valuable research tool for molecular biologists and virologists. Indeed, the establishment of a reverse genetics system for the recovery of infectious VSV from cDNA transformed the utility of this virus and paved the way for its use as a vaccine vector. A highly effective VSV-based vaccine against Ebola virus recently received clinical approval, and many other VSV-based vaccines have been developed, particularly for high-consequence viruses. This review seeks to provide a holistic but concise overview of VSV, covering the virus’s ascension from perennial agricultural scourge to promising medical countermeasure, with a particular focus on vaccines.

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Components and Architecture of the Rhabdovirus Ribonucleoprotein Complex

Cited by 21 publications

References 92 publications

Glycoproteins of Predicted Amphibian and Reptile Lyssaviruses Can Mediate Infection of Mammalian and Reptile Cells

Glycoproteins of Predicted Amphibian and Reptile Lyssaviruses Can Mediate Infection of Mammalian and Reptile Cells

Deconstructing virus condensation

Vesicular Stomatitis Virus: From Agricultural Pathogen to Vaccine Vector

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